Abstract
The metabolism of extracellular glutathione was studied in the isolated, perfused rat kidney. The results indicate different localization of glutathione oxidase and γ-glutamyltransferase ((5-glutamyl)-peptide: aminoacid 5-glutamyltransferase, EC 2.3.2.2) activities, since glutathione oxidase activity was observed only with glutathione present in the perfusate, whereas γ-glutamyltransferase-mediated metabolism of glutathione was restricted to glutathione present in the tubular fluid. Hence, the present findings are in accordance with previous observations in regard to the localization of renal γ-glutamyltransferase in the brush border membranes of the tubular epithelium, but suggest an opposite localization of renal glutathione oxidase activity, i.e., in the basal plasma membrane fraction of the tubular cells, facing the capillary bloodstream. Furthermore, the existence of a tubular glutathione extraction mechanism operating in addition to glomerular filtration is confirmed.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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